鲢鱼鳞胶原肽-铁螯合物的制备及其特性表征  

Preparation and Characterization of Iron-chelating Peptides from Silver Carp Scale Collagen

作　　者：熊喆 秦子波 赵钰 王希搏 荣建华[1] 熊善柏[1,2] 胡杨 XIONG Zhe;QIN Zibo;ZHAO Yu;WANG Xibo;RONG Jianhua;XIONG Shanbai;HU Yang(College of Food Science and Technology,National Bulk Freshwater Fish Processing Technology Research and Development Sub-center,Huazhong Agricultural University,Wuhan 430070,China;Bioactive Peptide Engineering Research Center,No.195 Dongfang Ave,Jingzhou 434000,China)

机构地区：[1]华中农业大学食品科学技术学院,国家大宗淡水鱼加工技术研发分中心,湖北武汉430070 [2]湖北省生物活性肽工程研究中心,湖北荆州434000

出　　处：《现代食品科技》2023年第4期187-195,共9页Modern Food Science and Technology

基　　金：湖北省自然科学基金面上项目(2022CFB162);湖北省重点研发计划项目(2021BBA089);中央高校基本科研业务费专项基金资助(2662018JC019)。

摘　　要：该研究将鲢鱼鳞胶原肽与亚铁离子进行螯合,以螯合率为评价指标,通过单因素实验结合响应面分析法,探究胶原肽-铁螯合物的最佳制备条件并对其分子量分布、氨基酸组成和结构进行表征。结果表明:胶原肽-铁螯合物的最佳制备条件为pH值7.5、肽铁质量比5:1、肽液质量分数2.5%、螯合时间40 min、螯合温度35℃,在此条件下,铁的螯合率为92.04%。由分子量分布和氨基酸组成分析可知,胶原肽与Fe2+螯后1000 u以下的分子量占比下降,胶原肽中存在的谷氨酸、天冬氨酸、丙氨酸、缬氨酸和精氨酸对螯合反应具有重要作用;紫外和红外光谱结果表明,胶原肽中的羧基、氨基和酰胺基等基团参与了螯合反应;X射线衍射图谱也显示鲢鱼鳞胶原肽-铁螯合物呈现出不同于胶原肽的非晶形结构。该研究可望为鲢鱼鳞胶原肽-铁螯合物的制备、工艺优选及结构表征提供参考。Silver carp scale collagen peptides were chelated with ferrous ions,with the chelation rate as an evaluation index.The optimum preparation conditions for the iron-chelating collagen peptides were explored and their molecular weight distribution,amino acid composition,and structure were characterized via single factor experiments and response surface analysis.The optimal preparation conditions for the iron-chelating collagen peptides were as follows:pH value,7.5;peptide-iron mass ratio,5:1;peptide solution mass fraction,2.5%;chelating time,40 min;and chelating temperature,35.Under these conditions,the chelation rate of iron was 92.04%.According to the analysis of molecular℃weight distribution and amino acid composition,after collagen peptide and Fe2+chelation,the proportion of molecular weight below 1000 u decreased,with glutamic acid,aspartic acid,alanine,valine,and arginine in the collagen peptides playing important roles in the chelation reaction.Furthermore,the X-ray diffraction patterns showed that iron-chelating peptides from silver carp scale collagen had an amorphous structure,unlike collagen peptide.This study is expected to serve as a reference for the preparation,optimization,and structural characterization of iron-chelating peptides from silver carp collagen.

关 键 词：鲢鱼鳞胶原肽 肽-铁螯合物 螯合率 工艺优化 结构表征 

分 类 号：TS254.9[轻工技术与工程—水产品加工及贮藏工程]